|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
3-347 |
1.22e-46 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 163.16 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 3 AMAAEEEVDSADAGGGSGWlTGWLP---TWCPTSTSHLKEAEEKMLKCVPCTYKKEPVRISNG----------------N 63
Cdd:PLN02894 14 GAASSAAASAAASAETSRT-RSLWPsplRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGppgskvrwfrsasnepR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 64 RIWTLMFSHNISSKTpLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRC 142
Cdd:PLN02894 93 FINTVTFDSKEDAPT-LVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 143 ALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGFPERPDlaDQERPI----PVWIRALGAAL--TPFNPLAGL 216
Cdd:PLN02894 172 AKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESD--DKSEWLtkfrATWKGAVLNHLweSNFTPQKII 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 217 RIAGPFGLSLVQRLRPDFKRKYS-----SMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGglHPDIP 291
Cdd:PLN02894 250 RGLGPWGPNLVRRYTTARFGAHStgdilSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVP 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 13385690 292 VSVIFGARSCIDgNSGTSIQSLRPKSYVKTIAILGAGHYVYADQPEEFNQKVKEIC 347
Cdd:PLN02894 328 TTFIYGRHDWMN-YEGAVEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYAC 382
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
93-336 |
1.38e-19 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 86.40 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 93 WALNFEDLSTDR-PVYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSR 171
Cdd:pfam00561 16 WRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 172 VSHLILVEPWG-FPERPDLADQERPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtv 247
Cdd:pfam00561 94 VKALVLLGALDpPHELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 248 teyiyhcnVQTPSGETAFKNMTIPYgWAKRPMLQRIGGLhpDIPVSVIFGARSCIDGNSGT-SIQSLRPKSYVKTIAilG 326
Cdd:pfam00561 169 --------YALAKSLVTGALLFIET-WSTELRAKFLGRL--DEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--D 235
|
250
....*....|
gi 13385690 327 AGHYVYADQP 336
Cdd:pfam00561 236 AGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
93-345 |
1.99e-18 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 82.74 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 93 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRV 172
Cdd:COG0596 39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 173 SHLILVepwgfperpdladqerpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 252
Cdd:COG0596 115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 253 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgglhpDIPVSVIFGARS-CIDGNSGTSIQSLRPKSYVKTIAilGAGHYV 331
Cdd:COG0596 130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202
|
250
....*....|....
gi 13385690 332 YADQPEEFNQKVKE 345
Cdd:COG0596 203 PLEQPEAFAAALRD 216
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
105-199 |
7.19e-06 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214007 Cd Length: 309 Bit Score: 47.24 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 105 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCAL--RLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPW 181
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDALldRVGPCIVVAHSQGGGFAFEAARARPDLVRAVVALEPS 222
|
90 100
....*....|....*....|.
gi 13385690 182 GFPERPDLADqERPIP---VW 199
Cdd:cd12808 223 GAPDPAEAAP-LADVPhllVW 242
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
3-347 |
1.22e-46 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 163.16 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 3 AMAAEEEVDSADAGGGSGWlTGWLP---TWCPTSTSHLKEAEEKMLKCVPCTYKKEPVRISNG----------------N 63
Cdd:PLN02894 14 GAASSAAASAAASAETSRT-RSLWPsplRWIPTSTDHIIAAEKRLLSLVKTPYVQEQVNIGSGppgskvrwfrsasnepR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 64 RIWTLMFSHNISSKTpLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDA-EEVENQFVESIEEWRC 142
Cdd:PLN02894 93 FINTVTFDSKEDAPT-LVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKStEETEAWFIDSFEEWRK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 143 ALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGFPERPDlaDQERPI----PVWIRALGAAL--TPFNPLAGL 216
Cdd:PLN02894 172 AKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSESD--DKSEWLtkfrATWKGAVLNHLweSNFTPQKII 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 217 RIAGPFGLSLVQRLRPDFKRKYS-----SMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGglHPDIP 291
Cdd:PLN02894 250 RGLGPWGPNLVRRYTTARFGAHStgdilSEEESKLLTDYVYHTLAAKASGELCLKYIFSFGAFARKPLLESAS--EWKVP 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 13385690 292 VSVIFGARSCIDgNSGTSIQSLRPKSYVKTIAILGAGHYVYADQPEEFNQKVKEIC 347
Cdd:PLN02894 328 TTFIYGRHDWMN-YEGAVEARKRMKVPCEIIRVPQGGHFVFLDNPSGFHSAVLYAC 382
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
93-336 |
1.38e-19 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 86.40 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 93 WALNFEDLSTDR-PVYAFDLLGFGRSSRPRFDSDAEEVEnqFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSR 171
Cdd:pfam00561 16 WRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDD--LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 172 VSHLILVEPWG-FPERPDLADQERPIPVWIR---ALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFeddtv 247
Cdd:pfam00561 94 VKALVLLGALDpPHELDEADRFILALFPGFFdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 248 teyiyhcnVQTPSGETAFKNMTIPYgWAKRPMLQRIGGLhpDIPVSVIFGARSCIDGNSGT-SIQSLRPKSYVKTIAilG 326
Cdd:pfam00561 169 --------YALAKSLVTGALLFIET-WSTELRAKFLGRL--DEPTLIIWGDQDPLVPPQALeKLAQLFPNARLVVIP--D 235
|
250
....*....|
gi 13385690 327 AGHYVYADQP 336
Cdd:pfam00561 236 AGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
93-345 |
1.99e-18 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 82.74 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 93 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEevenQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRV 172
Cdd:COG0596 39 WRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLD----DLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 173 SHLILVepwgfperpdladqerpipvwiralgaaltpfnplaglriagpfglslvqrlrpdfkrkyssmfeDDTVTEYIY 252
Cdd:COG0596 115 AGLVLV-----------------------------------------------------------------DEVLAALAE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 253 HCNVQTPSGETAFKNMTIPYGWAKRPMLQRIgglhpDIPVSVIFGARS-CIDGNSGTSIQSLRPKSYVKTIAilGAGHYV 331
Cdd:COG0596 130 PLRRPGLAPEALAALLRALARTDLRERLARI-----TVPTLVIWGEKDpIVPPALARRLAELLPNAELVVLP--GAGHFP 202
|
250
....*....|....
gi 13385690 332 YADQPEEFNQKVKE 345
Cdd:COG0596 203 PLEQPEAFAAALRD 216
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
106-206 |
9.60e-13 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 66.56 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 106 VYAFDLLGFGRSSRPRFDSDAEEvenQFVESIEEWRCALRLD---KMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWg 182
Cdd:COG2267 58 VLAFDLRGHGRSDGPRGHVDSFD---DYVDDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA- 133
|
90 100
....*....|....*....|....*
gi 13385690 183 fperpDLADQERPIPV-WIRALGAA 206
Cdd:COG2267 134 -----YRADPLLGPSArWLRALRLA 153
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
106-238 |
1.43e-12 |
|
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
Pssm-ID: 463473 [Multi-domain] Cd Length: 238 Bit Score: 66.47 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 106 VYAFDLLGFGRSSRPR--FDSDAEEVE--NQFVESI-EEWRCAlrldKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEP 180
Cdd:pfam12146 34 VYAYDHRGHGRSDGKRghVPSFDDYVDdlDTFVDKIrEEHPGL----PLFLLGHSMGGLIAALYALRYPDKVDGLILSAP 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 13385690 181 WgfperpdLADQERPIPVWIRALGAALTPFNPlaGLRIAGPFGLSLVQRlRPDFKRKY 238
Cdd:pfam12146 110 A-------LKIKPYLAPPILKLLAKLLGKLFP--RLRVPNNLLPDSLSR-DPEVVAAY 157
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
78-183 |
1.65e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 55.34 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 78 TPLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEvenqFVESIEEWRCALRLDKMILLGHNLG 157
Cdd:PRK14875 132 TPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAGSLDE----LAAAVLAFLDALGIERAHLVGHSMG 207
|
90 100
....*....|....*....|....*.
gi 13385690 158 GFLAAAYSLKYPSRVSHLILVEPWGF 183
Cdd:PRK14875 208 GAVALRLAARAPQRVASLTLIAPAGL 233
|
|
| PLN02578 |
PLN02578 |
hydrolase |
93-182 |
5.11e-07 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 50.99 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 93 WALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEwrcaLRLDKMILLGHNLGGFLAAAYSLKYPSRV 172
Cdd:PLN02578 102 WRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVWRDQVADFVKE----VVKEPAVLVGNSLGGFTALSTAVGYPELV 177
|
90
....*....|
gi 13385690 173 SHLILVEPWG 182
Cdd:PLN02578 178 AGVALLNSAG 187
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
100-341 |
7.88e-07 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 49.39 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 100 LSTDRPVYAFDLLGFGRSSRPRFD-SDAEEVENqFVESIEEWRCAlrldkmILLGHNLGGFLAAAYSlkyPSRVSHLILV 178
Cdd:pfam12697 18 LAAGVAVLAPDLPGHGSSSPPPLDlADLADLAA-LLDELGAARPV------VLVGHSLGGAVALAAA---AAALVVGVLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 179 EPWGFPerpdlADQERPIPVWIRALGAALtpfnplaglriaGPFGLSLVQRLRPDFKrkyssmfeDDTVTEYIYHCNVQT 258
Cdd:pfam12697 88 APLAAP-----PGLLAALLALLARLGAAL------------AAPAWLAAESLARGFL--------DDLPADAEWAAALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 259 PSGETAFKNMTIPYGWakrpmlqrigglhPDIPVSVIFGARSciDGNSGTSIQ-SLRPKSYVKTIAILGAGHYVYaDQPE 337
Cdd:pfam12697 143 LAALLAALALLPLAAW-------------RDLPVPVLVLAEE--DRLVPELAQrLLAALAGARLVVLPGAGHLPL-DDPE 206
|
....
gi 13385690 338 EFNQ 341
Cdd:pfam12697 207 EVAE 210
|
|
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
96-184 |
1.74e-06 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 49.42 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 96 NFEDLS-TDRPVYAFDLLGFGRSSRPrfdSDAEEVENQFVESIEewRCAL---RLDKMILLGHNLGGFLAAAYSLKYPSR 171
Cdd:PLN03087 224 NFSDAAkSTYRLFAVDLLGFGRSPKP---ADSLYTLREHLEMIE--RSVLeryKVKSFHIVAHSLGCILALALAVKHPGA 298
|
90
....*....|...
gi 13385690 172 VSHLILVEPWGFP 184
Cdd:PLN03087 299 VKSLTLLAPPYYP 311
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
105-199 |
7.19e-06 |
|
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.
Pssm-ID: 214007 Cd Length: 309 Bit Score: 47.24 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 105 PVYAFDllGFGRSSRPRF-DSDAeevenqfveSIEEWRCAL--RLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPW 181
Cdd:cd12808 154 PLAAFD--AFAKQFVPRWlGTDA---------LTLAAYDALldRVGPCIVVAHSQGGGFAFEAARARPDLVRAVVALEPS 222
|
90 100
....*....|....*....|.
gi 13385690 182 GFPERPDLADqERPIP---VW 199
Cdd:cd12808 223 GAPDPAEAAP-LADVPhllVW 242
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
100-180 |
9.31e-05 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 44.10 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 100 LSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALRLDKMILLGHnlGGFLAAA--YSLKYPSRVSHLIL 177
Cdd:PLN03084 150 LSKNYHAIAFDWLGFGFSDKPQPGYGFNYTLDEYVSSLESLIDELKSDKVSLVVQ--GYFSPPVvkYASAHPDKIKKLIL 227
|
...
gi 13385690 178 VEP 180
Cdd:PLN03084 228 LNP 230
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
93-178 |
5.68e-04 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 41.16 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 93 WALNF-------EDLSTDRPVYAFDLLGFGRSS---RPRFDSDAEEVENQfvesieewrcalRLDKMILLGHNLGGFLAA 162
Cdd:PRK10349 22 WGLNAevwrcidEELSSHFTLHLVDLPGFGRSRgfgALSLADMAEAVLQQ------------APDKAIWLGWSLGGLVAS 89
|
90
....*....|....*.
gi 13385690 163 AYSLKYPSRVSHLILV 178
Cdd:PRK10349 90 QIALTHPERVQALVTV 105
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
109-200 |
8.87e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 109 FDLLGF-GRSSRPRFDSDAEEVeNQFVESIEEwRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPwGFPERP 187
Cdd:COG0400 52 FDLSFLeGREDEEGLAAAAEAL-AAFIDELEA-RYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSG-YLPGEE 128
|
90
....*....|....*.
gi 13385690 188 DLADQE---RPIPVWI 200
Cdd:COG0400 129 ALPAPEaalAGTPVFL 144
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
108-196 |
2.86e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 39.21 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 108 AFDLLGFGRSSRP----RFDSDAeevenQFVESieeWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGF 183
Cdd:PRK03592 58 APDLIGMGASDKPdidyTFADHA-----RYLDA---WFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIVR 129
|
90
....*....|....
gi 13385690 184 PER-PDLADQERPI 196
Cdd:PRK03592 130 PMTwDDFPPAVREL 143
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
100-231 |
5.39e-03 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 38.92 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385690 100 LSTDRPVYAFDLLGFGRSSRPrfdsdaeevenqfVESIEEwRCALRLDKM---------ILLGHNLGGFLA--AAYSLKy 168
Cdd:COG3319 624 LGPDRPVYGLQAPGLDGGEPP-------------PASVEE-MAARYVEAIravqpegpyHLLGWSFGGLVAyeMARQLE- 688
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13385690 169 pSR---VSHLILVEPWGfPERPDLADQERPIPVWIRALGAALTPFNPLAGLRiagpfGLSLVQRLR 231
Cdd:COG3319 689 -AQgeeVALLVLLDSYA-PGALARLDEAELLAALLRDLARGVDLPLDAEELR-----ALDPEERLA 747
|
|
| |
